This paper reports experiments on the stereospecificity observed in the monophenolase and diphenolase activities of mushroom tyrosinase. Several enantiomorphs of monophenols and o-diphenols were assayed: l-tyrosine, d,l-tyrosine, d-tyrosine; l-α-methyltyrosine, d,l-α-methyltyrosine; l-dopa, d,l-dopa, d-dopa; l-α-methyldopa, d,l-α-methyldopa; l-isoprenaline, d,l-isoprenaline and d-isoprenaline. The Vmax values obtained for each series were the same. The electronic densities on the carbon atoms in the meta(C-3) and the para(C-4) positions of the benzene ring were determined by NMR assays. This value is related to the nucleophilic power of the oxygen atom belonging to the hydroxy group, which could explain the Vmax values experimentally obtained for the monophenolase and diphenolase activities of mushroom tyrosinase. The spatial orientation of the ring substituents led to lower Km values for l-isomers than for d-isomers. However, the Vmax values were the same for each series of isomers because spatial orientation did not affect the NMR value of C-4. Therefore mushroom tyrosinase showed stereospecificity in its affinity towards its substrates (Km) but not in the transformation reaction rate (Vmax) of these substrates.

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